A plausible identification of secondary binding site in trypsin and trypsinogen
Rev. bras. pesqui. méd. biol
; Braz. j. med. biol. res;23(12): 1223-31, 1990. tab
Article
em En
| LILACS
| ID: lil-103648
Biblioteca responsável:
BR1.1
RESUMO
1. The determination of the binding of 4,4'diazoamino-bis-benzamidine (DABB) to alfa-trypsin by equilibrium measurements in columns indicated a stoichiometry of 2 mol ligan/mol enzyme. One molecule binds to the secondy binding site, sith Ki2=mMat pH8,0, 25-C. 2. Bovine pancreatic trypsin inhibitor (BPTI) prevented binding of DABB to both sites, indicating that they are topographically close and within the interface of the trypsin-BPTI complex. 3. On the basis of data from the interface of the trypsin-BPTI complex, we concluded that the secondary binding site of trypsin is plausibly identified as the same site in trypsin that binds the Arg-17 reside of BPTI, i.e., Tyr-39 and Tyr-151 in bovine trypsin. This site would then correspond to subsite S'2 on the enzyme surface
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Índice:
LILACS
Assunto principal:
Benzamidinas
/
Tripsina
Tipo de estudo:
Diagnostic_studies
Idioma:
En
Revista:
Braz. j. med. biol. res
/
Rev. bras. pesqui. méd. biol
Assunto da revista:
BIOLOGIA
/
MEDICINA
Ano de publicação:
1990
Tipo de documento:
Article